ATP synthase subunit beta (P0ABB4)

Identification
Name:ATP synthase subunit beta
Synonyms:
  • ATP synthase F1 sector subunit beta
  • F-ATPase subunit beta
Gene Name:atpD
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits
Cellular Location:Cell inner membrane; Peripheral membrane protein
SMPDB Pathways:
  • Oxidative phosphorylation PW000919
  • purine nucleotides de novo biosynthesis PW000910
  • purine nucleotides de novo biosynthesis 1435709748 PW000960
  • purine nucleotides de novo biosynthesis 2 PW002033
KEGG Pathways:
SMPDB Reactions:
1.0Adenosine diphosphate+1.0Thumb+4.0Thumb+1.0Thumb ↔ 1.0Thumb+3.0Thumb+1.0Thumb
1.0Adenosine diphosphate + 1.0Phosphate + 4.0Hydrogen ion + 1.0ADP ↔ 1.0Water + 3.0Hydrogen ion + 1.0Adenosine triphosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
macromolecular complex
protein complex
proton-transporting ATP synthase complex, catalytic core F(1)
proton-transporting two-sector ATPase complex
proton-transporting two-sector ATPase complex, catalytic domain
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
cation transmembrane transporter activity
hydrogen ion transmembrane transporter activity
hydrogen ion transporting ATP synthase activity, rotational mechanism
hydrogen-exporting ATPase activity, phosphorylative mechanism
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
inorganic cation transmembrane transporter activity
ion transmembrane transporter activity
monovalent inorganic cation transmembrane transporter activity
nucleoside binding
nucleoside-triphosphatase activity
nucleotide binding
proton-transporting ATPase activity, rotational mechanism
purine nucleoside binding
pyrophosphatase activity
substrate-specific transmembrane transporter activity
transmembrane transporter activity
transporter activity
Process
ATP biosynthetic process
ATP metabolic process
ATP synthesis coupled proton transport
cellular nitrogen compound metabolic process
establishment of localization
hydrogen transport
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
proton transport
purine nucleoside triphosphate biosynthetic process
purine nucleoside triphosphate metabolic process
purine nucleotide biosynthetic process
purine nucleotide metabolic process
purine ribonucleoside triphosphate biosynthetic process
purine ribonucleoside triphosphate metabolic process
transport
Gene Properties
Blattner:b3732
Gene OrientationCounterclockwise
Centisome Percentage:84.36
Left Sequence End3914016
Right Sequence End3915398
Gene Sequence:
>1383 bp
ATGACGCAATTAACCATGAAAGACAAAATTGGCTACGGGCTGGGAGACACCGCCTGCGGC
TTCGTCTGGCAGGCCACGATGTTCCTGCTGGCCTATTTCTACACCGACGTCTTCGGCCTG
TCGGCGGGGATTATGGGCACGCTGTTTTTGGTCTCCCGCGTGCTCGACGCCGTCACCGAC
CCGCTGATGGGGCTGCTGGTAGACCGCACCCGCACGCGGCACGGCCAGTTCCGCCCGTTC
CTGCTGTGGGGGGCCATCCCGTTCGGCATCGTCTGCGTGCTGACCTTCTACACGCCGGAC
TTCTCCGCACAGGGCAAGATCATCTACGCCTGCGTGACCTACATTCTCCTGACCCTGGTC
TACACCTTCGTTAACGTGCCGTACTGCGCCATGCCGGGCGTCATCACCGCCGACCCGAAA
GAGCGTCACGCCCTGCAGTCCTGGCGCTTCTTCCTGGCGGCGGCGGGCTCGCTCGCTATC
AGCGGCATCGCGCTGCCGCTGGTGAGCATCATCGGCAAAGGGGACGAGCAGGTGGGCTAC
TTCGGCGCCATGTGCGTGCTGGGGCTGAGCGGCGTGGTGCTGCTCTACGTCTGCTTCTTC
ACGACCAAAGAGCGCTACACCTTTGAGGTGCAGCCGGGCTCGTCGGTGGCGAAAGACCTT
AAGCTGCTGCTGGGCAACAGCCAGTGGCGCATCATGTGCGCGTTCAAGATGATGGCGACC
TGCTCCAACGTGGTGCGCGGCGGGGCGACGCTCTACTTCGTGAAATACGTGATGGATCAC
CCGGAGTTGGCGACCCAGTTTTTACTTTACGGCAGCCTCGCCACCATGTTCGGCTCGCTT
TGCTCCTCACGCCTGCTGGGCCGCTTCGACCGCGTCACCGCCTTCAAGTGGATCATCGTC
GCCTACTCGCTGATCAGCCTGCTGATTTTCGTCACCCCGGCGGAGCACATCGCGCTCATT
TTTGCCCTCAACATCCTGTTCCTGTTCGTCTTTAATACCACCACGCCGCTGCAGTGGCTG
ATGGCTTCTGACGTGGTGGACTACGAGGAGAGCCGCAGCGGTCGCCGCCTCGACGGGCTG
GTGTTCTCCACCTACCTGTTCAGCCTGAAGATTGGCCTGGCGATTGGCGGGGCGGTGGTG
GGCTGGATCCTGGCGTACGTCAACTATTCCGCCAGCAGCAGCGTGCAGCCGGTTGAGGTG
CTCACCACCATCAAAATTCTGTTCTGCGTGGTGCCGGTGGTGCTCTACGCGGGCATGTTC
ATCATGCTGTCGCTCTACAAGCTCACCGATGCCCGCGTGGAGGCCATCAGCCGGCAGCTG
ATTAAGCACCGCGCGGCGCAGGGCGAGGCCGTTCCCGACGCCGCGACAGCCGCATCCCAT
TAA
Protein Properties
Pfam Domain Function:
Protein Residues:460
Protein Molecular Weight:50325
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>ATP synthase subunit beta
MATGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNERLVLEVQQQLGGGIVRTIAMGSS
DGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEEL
SNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGV
GERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLL
FVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVP
ADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDTARG
VQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLSQPFFVAEVFTGSPGKYVS
LKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEEAVEKAKKL
References
External Links:
ResourceLink
Uniprot ID:P0ABB4
Uniprot Name:ATPB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674414
Ecogene ID:EG10101
Ecocyc:EG10101
ColiBase:b3732
Kegg Gene:b3732
EchoBASE ID:EB0099
CCDB:ATPB_ECOLI
BacMap:16131600
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
  • Hausrath, A. C., Gruber, G., Matthews, B. W., Capaldi, R. A. (1999). "Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallography." Proc Natl Acad Sci U S A 96:13697-13702. Pubmed: 10570135
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Iwamoto, A., Omote, H., Hanada, H., Tomioka, N., Itai, A., Maeda, M., Futai, M. (1991). "Mutations in Ser174 and the glycine-rich sequence (Gly149, Gly150, and Thr156) in the beta subunit of Escherichia coli H(+)-ATPase." J Biol Chem 266:16350-16355. Pubmed: 1832155
  • Kanazawa, H., Futai, M. (1982). "Structure and function of H+-ATPase: what we have learned from Escherichia coli H+-ATPase." Ann N Y Acad Sci 402:45-64. Pubmed: 6301339
  • Kanazawa, H., Kayano, T., Kiyasu, T., Futai, M. (1982). "Nucleotide sequence of the genes for beta and epsilon subunits of proton-translocating ATPase from Escherichia coli." Biochem Biophys Res Commun 105:1257-1264. Pubmed: 6285901
  • Kanazawa, H., Kayano, T., Mabuchi, K., Futai, M. (1981). "Nucleotide sequence of the genes coding for alpha, beta and gamma subunits of the proton-translocating ATPase of Escherichia coli." Biochem Biophys Res Commun 103:604-612. Pubmed: 6277310
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Saraste, M., Gay, N. J., Eberle, A., Runswick, M. J., Walker, J. E. (1981). "The atp operon: nucleotide sequence of the genes for the gamma, beta, and epsilon subunits of Escherichia coli ATP synthase." Nucleic Acids Res 9:5287-5296. Pubmed: 6272217
  • Walker, J. E., Gay, N. J., Saraste, M., Eberle, A. N. (1984). "DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS." Biochem J 224:799-815. Pubmed: 6395859
  • Wise, J. G., Hicke, B. J., Boyer, P. D. (1987). "Catalytic and noncatalytic nucleotide binding sites of the Escherichia coli F1 ATPase. Amino acid sequences of beta-subunit tryptic peptides labeled with 2-azido-ATP." FEBS Lett 223:395-401. Pubmed: 2889623